Chaperonin turned insect toxin

Naofumi Yoshida, Kenji Oeda, Eijiro Watanabe, Toshiyuki Mikami, Yoshikazu Fukita, Keiichiro Nishimura, Koichiro Komai and Kazuhiko Matsuda ()
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Naofumi Yoshida: Faculty of Agriculture, Kinki University
Kenji Oeda: Agricultural Chemicals Research Laboratory
Eijiro Watanabe: Genomic Science Laboratories, Sumitomo Pharmaceuticals
Toshiyuki Mikami: Genomic Science Laboratories, Sumitomo Pharmaceuticals
Yoshikazu Fukita: Organic Synthesis Research Laboratory, Sumitomo Chemical Co.
Keiichiro Nishimura: Research Institute for Advanced Science and Technology, Osaka Prefecture University
Koichiro Komai: Faculty of Agriculture, Kinki University
Kazuhiko Matsuda: Faculty of Agriculture, Kinki University

Nature, 2001, vol. 411, issue 6833, 44-44

Abstract: Abstract Antlions are larvae of the Myrmeleontidae family that live on other insects1 by sucking out the body fluid from their prey, after first paralysing it with a toxin produced by salivary bacteria. Here we show that the paralysing toxin produced by bacterial endosymbionts in the saliva of Myrmeleon bore larvae is a homologue of GroEL, a protective heat-shock protein known as a molecular chaperone. The amino-acid residues critical for this protein's toxicity are located away from the regions essential to its protein-folding activity, indicating that the dual function of this GroEL homologue may benefit both the antlion and the endosymbiont.

Date: 2001
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DOI: 10.1038/35075148

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